메뉴 건너뛰기




Volumn 1773, Issue 9, 2007, Pages 1473-1482

Oxidative stress-induced expression and modulation of Phosphatase of Regenerating Liver-1 (PRL-1) in mammalian retina

Author keywords

Cysteine; Light damage; Oxidation reduction; Phosphatase; Photoreceptor; Retina

Indexed keywords

CYCLOHEXIMIDE; CYSTEINE; GLUTATHIONE; HYDROGEN PEROXIDE; PROTEIN TYROSINE PHOSPHATASE;

EID: 34548498188     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.06.005     Document Type: Article
Times cited : (27)

References (59)
  • 1
    • 0034646902 scopus 로고    scopus 로고
    • Expression of the protein tyrosine phosphatase, phosphatase of regenerating liver 1, in the outer segments of primate cone photoreceptors
    • Yarovinsky T.O., Rickman D.W., Diamond R.H., Taub R., Hageman G.S., and Bowes Rickman C. Expression of the protein tyrosine phosphatase, phosphatase of regenerating liver 1, in the outer segments of primate cone photoreceptors. Brain Res. Mol. Brain Res. 77 (2000) 95-103
    • (2000) Brain Res. Mol. Brain Res. , vol.77 , pp. 95-103
    • Yarovinsky, T.O.1    Rickman, D.W.2    Diamond, R.H.3    Taub, R.4    Hageman, G.S.5    Bowes Rickman, C.6
  • 2
    • 0032479428 scopus 로고    scopus 로고
    • The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer
    • Peng Y., Genin A., Spinner N.B., Diamond R.H., and Taub R. The gene encoding human nuclear protein tyrosine phosphatase, PRL-1. Cloning, chromosomal localization, and identification of an intron enhancer. J. Biol. Chem. 273 (1998) 17286-17295
    • (1998) J. Biol. Chem. , vol.273 , pp. 17286-17295
    • Peng, Y.1    Genin, A.2    Spinner, N.B.3    Diamond, R.H.4    Taub, R.5
  • 3
    • 0031874062 scopus 로고    scopus 로고
    • Assessment of the interphotoreceptor matrix proteoglycan-1 (IMPG1) gene localised to 6q13-q15 in autosomal dominant Stargardt-like disease (ADSTGD), progressive bifocal chorioretinal atrophy (PBCRA), and North Carolina macular dystrophy (MCDR1)
    • Gehrig A., Felbor U., Kelsell R.E., Hunt D.M., Maumenee I.H., and Weber B.H. Assessment of the interphotoreceptor matrix proteoglycan-1 (IMPG1) gene localised to 6q13-q15 in autosomal dominant Stargardt-like disease (ADSTGD), progressive bifocal chorioretinal atrophy (PBCRA), and North Carolina macular dystrophy (MCDR1). J. Med. Genet. 35 (1998) 641-645
    • (1998) J. Med. Genet. , vol.35 , pp. 641-645
    • Gehrig, A.1    Felbor, U.2    Kelsell, R.E.3    Hunt, D.M.4    Maumenee, I.H.5    Weber, B.H.6
  • 4
    • 0028359370 scopus 로고
    • PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
    • Diamond R.H., Cressman D.E., Laz T.M., Abrams C.S., and Taub R. PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth. Mol. Cell. Biol. 14 (1994) 3752-3762
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3752-3762
    • Diamond, R.H.1    Cressman, D.E.2    Laz, T.M.3    Abrams, C.S.4    Taub, R.5
  • 5
    • 0032539752 scopus 로고    scopus 로고
    • Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1
    • Zeng Q., Hong W., and Tan Y.H. Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1. Biochem. Biophys. Res. Commun. 244 (1998) 421-427
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 421-427
    • Zeng, Q.1    Hong, W.2    Tan, Y.H.3
  • 8
    • 0034647510 scopus 로고    scopus 로고
    • Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome
    • Zeng Q., Si X., Horstmann H., Xu Y., Hong W., and Pallen C.J. Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. J. Biol. Chem. 275 (2000) 21444-21452
    • (2000) J. Biol. Chem. , vol.275 , pp. 21444-21452
    • Zeng, Q.1    Si, X.2    Horstmann, H.3    Xu, Y.4    Hong, W.5    Pallen, C.J.6
  • 9
    • 1642482862 scopus 로고    scopus 로고
    • Structural insights into molecular function of the metastasis-associated phosphatase PRL-3
    • Kozlov G., Cheng J., Ziomek E., Banville D., Gehring K., and Ekiel I. Structural insights into molecular function of the metastasis-associated phosphatase PRL-3. J. Biol. Chem. 279 (2004) 11882-11889
    • (2004) J. Biol. Chem. , vol.279 , pp. 11882-11889
    • Kozlov, G.1    Cheng, J.2    Ziomek, E.3    Banville, D.4    Gehring, K.5    Ekiel, I.6
  • 10
    • 9644295701 scopus 로고    scopus 로고
    • Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms
    • Jeong D.G., Kim S.J., Kim J.H., Son J.H., Park M.R., Lim S.M., Yoon T.S., and Ryu S.E. Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. J. Mol. Biol. 345 (2005) 401-413
    • (2005) J. Mol. Biol. , vol.345 , pp. 401-413
    • Jeong, D.G.1    Kim, S.J.2    Kim, J.H.3    Son, J.H.4    Park, M.R.5    Lim, S.M.6    Yoon, T.S.7    Ryu, S.E.8
  • 11
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T., and Dixon J.E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273 (1998) 13375-13378
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 12
    • 0028359370 scopus 로고
    • PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
    • Diamond R.H., Cressman D.E., Laz T.M., Abrams C.S., and Taub R. PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth. Mol. Cell. Biol. 14 (1994) 3752-3762
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3752-3762
    • Diamond, R.H.1    Cressman, D.E.2    Laz, T.M.3    Abrams, C.S.4    Taub, R.5
  • 13
    • 0030221650 scopus 로고    scopus 로고
    • PRL-1, a protein tyrosine phosphatase, is expressed in neurons and oligodendrocytes in the brain and induced in the cerebral cortex following transient forebrain ischemia
    • Takano S., Fukuyama H., Fukumoto M., Kimura J., Xue J.H., Ohashi H., and Fujita J. PRL-1, a protein tyrosine phosphatase, is expressed in neurons and oligodendrocytes in the brain and induced in the cerebral cortex following transient forebrain ischemia. Brain Res. Mol. Brain Res. 40 (1996) 105-115
    • (1996) Brain Res. Mol. Brain Res. , vol.40 , pp. 105-115
    • Takano, S.1    Fukuyama, H.2    Fukumoto, M.3    Kimura, J.4    Xue, J.H.5    Ohashi, H.6    Fujita, J.7
  • 15
    • 0032497814 scopus 로고    scopus 로고
    • Expression of a novel rat protein tyrosine phosphatase gene
    • Carter D.A. Expression of a novel rat protein tyrosine phosphatase gene. Biochim. Biophys. Acta 1442 (1998) 405-408
    • (1998) Biochim. Biophys. Acta , vol.1442 , pp. 405-408
    • Carter, D.A.1
  • 16
    • 0033134685 scopus 로고    scopus 로고
    • Developmental expression of the murine Prl-1 protein tyrosine phosphatase gene
    • Rundle C.H., and Kappen C. Developmental expression of the murine Prl-1 protein tyrosine phosphatase gene. J. Exp. Zool. 283 (1999) 612-617
    • (1999) J. Exp. Zool. , vol.283 , pp. 612-617
    • Rundle, C.H.1    Kappen, C.2
  • 17
    • 0037195808 scopus 로고    scopus 로고
    • The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis
    • Wang J., Kirby C.E., and Herbst R. The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis. J. Biol. Chem. 277 (2002) 46659-46668
    • (2002) J. Biol. Chem. , vol.277 , pp. 46659-46668
    • Wang, J.1    Kirby, C.E.2    Herbst, R.3
  • 18
    • 0035957993 scopus 로고    scopus 로고
    • ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase
    • Peters C.S., Liang X., Li S., Kannan S., Peng Y., Taub R., and Diamond R.H. ATF-7, a novel bZIP protein, interacts with the PRL-1 protein-tyrosine phosphatase. J. Biol. Chem. 276 (2001) 13718-13726
    • (2001) J. Biol. Chem. , vol.276 , pp. 13718-13726
    • Peters, C.S.1    Liang, X.2    Li, S.3    Kannan, S.4    Peng, Y.5    Taub, R.6    Diamond, R.H.7
  • 19
    • 2342528447 scopus 로고    scopus 로고
    • Expression of pro-inflammatory markers by human dermal fibroblasts in a three-dimensional culture model is mediated by an autocrine interleukin-1 loop
    • Kessler-Becker D., Krieg T., and Eckes B. Expression of pro-inflammatory markers by human dermal fibroblasts in a three-dimensional culture model is mediated by an autocrine interleukin-1 loop. Biochem. J. 379 (2004) 351-358
    • (2004) Biochem. J. , vol.379 , pp. 351-358
    • Kessler-Becker, D.1    Krieg, T.2    Eckes, B.3
  • 21
    • 0033582426 scopus 로고    scopus 로고
    • Mitogenic up-regulation of the PRL-1 protein-tyrosine phosphatase gene by Egr-1. Egr-1 activation is an early event in liver regeneration
    • Peng Y., Du K., Ramirez S., Diamond R.H., and Taub R. Mitogenic up-regulation of the PRL-1 protein-tyrosine phosphatase gene by Egr-1. Egr-1 activation is an early event in liver regeneration. J. Biol. Chem. 274 (1999) 4513-4520
    • (1999) J. Biol. Chem. , vol.274 , pp. 4513-4520
    • Peng, Y.1    Du, K.2    Ramirez, S.3    Diamond, R.H.4    Taub, R.5
  • 22
    • 1342308079 scopus 로고    scopus 로고
    • Redox regulation of PTEN and protein tyrosine phosphatases in H(2)O(2) mediated cell signaling
    • Cho S.H., Lee C.H., Ahn Y., Kim H., Kim H., Ahn C.Y., Yang K.S., and Lee S.R. Redox regulation of PTEN and protein tyrosine phosphatases in H(2)O(2) mediated cell signaling. FEBS Lett. 560 (2004) 7-13
    • (2004) FEBS Lett. , vol.560 , pp. 7-13
    • Cho, S.H.1    Lee, C.H.2    Ahn, Y.3    Kim, H.4    Kim, H.5    Ahn, C.Y.6    Yang, K.S.7    Lee, S.R.8
  • 24
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman H.J., Fukuto J.M., and Torres M. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am. J. Physiol.: Cell Physiol. 287 (2004) C246-C256
    • (2004) Am. J. Physiol.: Cell Physiol. , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 25
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng T.C., Fukada T., and Tonks N.K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9 (2002) 387-399
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 26
    • 0037058883 scopus 로고    scopus 로고
    • Catalytic mechanism of Cdc25
    • Rudolph J. Catalytic mechanism of Cdc25. Biochemistry 41 (2002) 14613-14623
    • (2002) Biochemistry , vol.41 , pp. 14613-14623
    • Rudolph, J.1
  • 27
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen A., Andersen J.N., Myers M.P., Meng T.C., Hinks J.A., Tonks N.K., and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 31
    • 2342466682 scopus 로고    scopus 로고
    • Sunlight and the 10-year incidence of age-related maculopathy: the Beaver Dam Eye Study
    • Tomany S.C., Cruickshanks K.J., Klein R., Klein B.E., and Knudtson M.D. Sunlight and the 10-year incidence of age-related maculopathy: the Beaver Dam Eye Study. Arch. Ophthalmol. 122 (2004) 750-757
    • (2004) Arch. Ophthalmol. , vol.122 , pp. 750-757
    • Tomany, S.C.1    Cruickshanks, K.J.2    Klein, R.3    Klein, B.E.4    Knudtson, M.D.5
  • 34
    • 24644519820 scopus 로고    scopus 로고
    • Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion(,)
    • Sun J.P., Wang W.Q., Yang H., Liu S., Liang F., Fedorov A.A., Almo S.C., and Zhang Z.Y. Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion(,). Biochemistry 44 (2005) 12009-12021
    • (2005) Biochemistry , vol.44 , pp. 12009-12021
    • Sun, J.P.1    Wang, W.Q.2    Yang, H.3    Liu, S.4    Liang, F.5    Fedorov, A.A.6    Almo, S.C.7    Zhang, Z.Y.8
  • 35
    • 13644252192 scopus 로고    scopus 로고
    • 6,8-Difluoro-4-methylumbiliferyl phosphate: a fluorogenic substrate for protein tyrosine phosphatases
    • Welte S., Baringhaus K.H., Schmider W., Muller G., Petry S., and Tennagels N. 6,8-Difluoro-4-methylumbiliferyl phosphate: a fluorogenic substrate for protein tyrosine phosphatases. Anal. Biochem. 338 (2005) 32-38
    • (2005) Anal. Biochem. , vol.338 , pp. 32-38
    • Welte, S.1    Baringhaus, K.H.2    Schmider, W.3    Muller, G.4    Petry, S.5    Tennagels, N.6
  • 37
    • 0041323072 scopus 로고    scopus 로고
    • Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction
    • Sohn J., and Rudolph J. Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction. Biochemistry 42 (2003) 10060-10070
    • (2003) Biochemistry , vol.42 , pp. 10060-10070
    • Sohn, J.1    Rudolph, J.2
  • 38
    • 1542742250 scopus 로고    scopus 로고
    • Expression of cone-photoreceptor-specific antigens in a cell line derived from retinal tumors in transgenic mice
    • Tan E., Ding X.Q., Saadi A., Agarwal N., Naash M.I., and Al-Ubaidi M.R. Expression of cone-photoreceptor-specific antigens in a cell line derived from retinal tumors in transgenic mice. Invest. Ophthalmol. Visual Sci. 45 (2004) 764-768
    • (2004) Invest. Ophthalmol. Visual Sci. , vol.45 , pp. 764-768
    • Tan, E.1    Ding, X.Q.2    Saadi, A.3    Agarwal, N.4    Naash, M.I.5    Al-Ubaidi, M.R.6
  • 39
    • 0037036358 scopus 로고    scopus 로고
    • Reversible inactivation of the tumor suppressor PTEN by H2O2
    • Lee S.R., Yang K.S., Kwon J., Lee C., Jeong W., and Rhee S.G. Reversible inactivation of the tumor suppressor PTEN by H2O2. J. Biol. Chem. 277 (2002) 20336-20342
    • (2002) J. Biol. Chem. , vol.277 , pp. 20336-20342
    • Lee, S.R.1    Yang, K.S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 41
    • 34548510117 scopus 로고    scopus 로고
    • Rapid, reproducible Real-Time Quantitative RT-PCR using the iCycler iQ Real-Time PCR Detection System and iQ Supermix
    • Ebright J.N., and Bowes Rickman C. Rapid, reproducible Real-Time Quantitative RT-PCR using the iCycler iQ Real-Time PCR Detection System and iQ Supermix. BioRadiations 110 (2003) 32-35
    • (2003) BioRadiations , vol.110 , pp. 32-35
    • Ebright, J.N.1    Bowes Rickman, C.2
  • 42
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • (RESEARCH0034)
    • Vandesompele J., De Preter K., Pattyn F., Poppe B., Van Roy N., De Paepe A., and Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3 (2002) (RESEARCH0034)
    • (2002) Genome Biol. , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 43
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25 (2001) 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 44
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis
    • Zhang Z.Y. Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis. Crit. Rev. Biochem. Mol. Biol. 33 (1998) 1-52
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 1-52
    • Zhang, Z.Y.1
  • 45
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: mechanisms of catalysis and regulation
    • Denu J.M., and Dixon J.E. Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr. Opin. Chem. Biol. 2 (1998) 633-641
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 633-641
    • Denu, J.M.1    Dixon, J.E.2
  • 46
    • 0030297891 scopus 로고    scopus 로고
    • Form and function in protein dephosphorylation
    • Denu J.M., Stuckey J.A., Saper M.A., and Dixon J.E. Form and function in protein dephosphorylation. Cell 87 (1996) 361-364
    • (1996) Cell , vol.87 , pp. 361-364
    • Denu, J.M.1    Stuckey, J.A.2    Saper, M.A.3    Dixon, J.E.4
  • 47
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford D., Flint A.J., and Tonks N.K. Crystal structure of human protein tyrosine phosphatase 1B. Science 263 (1994) 1397-1404
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 48
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu J.M., and Tanner K.G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37 (1998) 5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 52
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • Claiborne A., Miller H., Parsonage D., and Ross R.P. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J. 7 (1993) 1483-1490
    • (1993) FASEB J. , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 54
    • 0035823539 scopus 로고    scopus 로고
    • Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation
    • Chiarugi P., Fiaschi T., Taddei M.L., Talini D., Giannoni E., Raugei G., and Ramponi G. Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation. J. Biol. Chem. 276 (2001) 33478-33487
    • (2001) J. Biol. Chem. , vol.276 , pp. 33478-33487
    • Chiarugi, P.1    Fiaschi, T.2    Taddei, M.L.3    Talini, D.4    Giannoni, E.5    Raugei, G.6    Ramponi, G.7
  • 55
    • 0033795036 scopus 로고    scopus 로고
    • The role of oxidative stress in the pathogenesis of age-related macular degeneration
    • Beatty S., Koh H., Phil M., Henson D., and Boulton M. The role of oxidative stress in the pathogenesis of age-related macular degeneration. Surv. Ophthalmol. 45 (2000) 115-134
    • (2000) Surv. Ophthalmol. , vol.45 , pp. 115-134
    • Beatty, S.1    Koh, H.2    Phil, M.3    Henson, D.4    Boulton, M.5
  • 56
    • 33644675223 scopus 로고    scopus 로고
    • Anatomy and development of the macula: specialisation and the vulnerability to macular degeneration
    • Provis J.M., Penfold P.L., Cornish E.E., Sandercoe T.M., and Madigan M.C. Anatomy and development of the macula: specialisation and the vulnerability to macular degeneration. Clin. Exp. Optom. 88 (2005) 269-281
    • (2005) Clin. Exp. Optom. , vol.88 , pp. 269-281
    • Provis, J.M.1    Penfold, P.L.2    Cornish, E.E.3    Sandercoe, T.M.4    Madigan, M.C.5
  • 57
    • 0023278631 scopus 로고
    • Effect of light history on retinal antioxidants and light damage susceptibility in the rat
    • Penn J.S., Naash M.I., and Anderson R.E. Effect of light history on retinal antioxidants and light damage susceptibility in the rat. Exp. Eye Res. 44 (1987) 779-788
    • (1987) Exp. Eye Res. , vol.44 , pp. 779-788
    • Penn, J.S.1    Naash, M.I.2    Anderson, R.E.3
  • 59
    • 3142721782 scopus 로고    scopus 로고
    • Induction of phase 2 genes by sulforaphane protects retinal pigment epithelial cells against photooxidative damage
    • Gao X., and Talalay P. Induction of phase 2 genes by sulforaphane protects retinal pigment epithelial cells against photooxidative damage. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 10446-10451
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10446-10451
    • Gao, X.1    Talalay, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.